Peptides

Amyloid-Forming Peptide GNNQQNY - 1 mg

  • Cat.Number : AS-62762
  • Availability :
    In stock

Quantity

This is a heptapeptide from the N-terminal prion-determining domain of the yeast protein Sup35 that forms amyloid fibrils. The availability of its detailed atomic oligomeric structure makes it a good model for studying the early stage of aggregation. The GNNQQNY dimer forms three stable sheet structures. in-register parallel, off-register parallel, and anti-parallel. The in-register parallel dimer, which is close to the amyloid beta-sheet structure, has few interpeptide hydrogen bonds, making hydrophobic interactions more important and increasing the conformational entropy compared to the anti-parallel sheet.

Specifications

Chemistry
Sequence one letter code
  • GNNQQNY
Sequence three letter code
  • H-Gly-Asn-Asn-Gln-Gln-Asn-Tyr-OH
Molecular Formula
  • C33H48N12O14
Molecular Mass/ Weight
  • 836.9
Modification
Conjugation
  • Unconjugated
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C
Activity
Biomarker Target
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • yeast

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Citations

Structure of the cross-β spine of amyloid-like fibrils.

Nature . 2005 Jun 09 ; 435(7043) 773 | DOI : 10.1038/nature03680

  • R. Nelson

References

Molecular Dynamics Simulations on the Oligomer-Formation Process of the GNNQQNY Peptide from Yeast Prion Protein Sup35

Biophys J . 2007 Sep 01 ; 93(5) 1484 | DOI : https://doi.org/10.1529/biophysj.106.100537

  • Z. Zhang
  • et al

Thermodynamics and Kinetics of Aggregation for the GNNQQNY Peptide

J. Am. Chem. Soc. . 2007 Dec 04 ; 129(51) 16005 | DOI : https://doi.org/10.1021/ja075346p

  • B. Strodel
  • et al

Structural Stability and Dynamics of an Amyloid-Forming Peptide GNNQQNY from the Yeast Prion Sup-35

Biophys. J . 2006 Aug 15 ; 91(3) 824 | DOI : https://doi.org/10.1529/biophysj.106.083246

  • J. Zheng
  • et al